ID I3MKN0_ICTTR Unreviewed; 1298 AA.
AC I3MKN0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Zinc finger protein 536 {ECO:0000313|Ensembl:ENSSTOP00000011881.3};
GN Name=ZNF536 {ECO:0000313|Ensembl:ENSSTOP00000011881.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000011881.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000011881.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000256|ARBA:ARBA00006991}.
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DR EMBL; AGTP01063098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01063099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01063100; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01063101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01063102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01063103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01063104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01063105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01063106; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01063107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005330700.1; XM_005330643.1.
DR STRING; 43179.ENSSTOP00000011881; -.
DR Ensembl; ENSSTOT00000013256.3; ENSSTOP00000011881.3; ENSSTOG00000013259.3.
DR GeneID; 101957640; -.
DR CTD; 9745; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156397; -.
DR HOGENOM; CLU_370320_0_0_1; -.
DR InParanoid; I3MKN0; -.
DR OrthoDB; 3849084at2759; -.
DR TreeFam; TF332241; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044323; F:retinoic acid-responsive element binding; IEA:Ensembl.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; IEA:Ensembl.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 6.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR45925; ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR45925:SF2; ZINC FINGER PROTEIN 536; 1.
DR Pfam; PF00096; zf-C2H2; 5.
DR Pfam; PF16606; zf-C2H2_assoc; 1.
DR Pfam; PF13909; zf-H2C2_5; 1.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 130..157
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 158..180
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 274..302
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 345..372
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 373..400
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 631..658
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 751..778
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 779..806
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1298 AA; 140940 MW; 06A2A65076216359 CRC64;
MEEASLCLGV SSAAPEAEPH LSGPVLNGQY AMSQKLHQIT SQLSHAFPEL HPRPNPEEKT
PAPLDEKSHV PMSGQPMGSQ MALLANQLGR DVDTSLNGRV DLQQFLNGQN LGIMSQMSDI
EDDARKNRKY PCPLCGKRFR FNSILSLHMR THTGEKPFKC PYCDHRAAQK GNLKIHLRTH
KLGNLGKGRG RVREENRLLH ELEERAILRD KQMKSSLLQP RADLKPLQHA QQAPLAACNL
ALPANHSVPD VANPVPSPKP TSVQEDAVAP AAGFRCTFCK GKFKKREELD RHIRILHKPY
KCTLCDFAAS QEEELISHVE KAHITAESAQ GQGPNAGGEQ SANEFRCEVC GQVFSQAWFL
KGHMRKHKDS FEHCCQICGR RFKEPWFLKN HMKVHLNKLS VKNKSPSEPE VPVSMGSMSQ
EAHANLYSRY LSCLQSGFMA PDKASLSEPS QLYGKGELPM KEKEVLGKLL SPISSMAHGV
PEGDKHSLLG CLNLVPPLKS SCIERLQAAA KAAEMDPVNS YQAWQLMARG MAMEHGFLSK
EHQLQRNHED TLANAGVMFD KEKREYVLVG ADGSKQKMPA DLVHSTKVGN QRDLPNKLDP
LEGSREFLSH GLNQTLEYNL QGPGNMKEKP TECPDCGRVF RTYHQVVVHS RVHKRDRKGD
EDGLHAGLDE RRGSGSDQES QSVSRSTTPG SSNVTEESGV GGGLSQTGSA QEDSPHPSSP
SSSDIGEEAG RSAGVQQPAL LRDRSLGSAM KDCPYCGKTF RTSHHLKVHL RIHTGEKPYK
CPHCDYAGTQ SASLKYHLER HHRERQNGAG PLSGQPPNQD HKDEMSSKAS LFIRPDILRG
AFKGLPGIDF RGGPASQQWT SGVISSGDHS GQATGMSSEA PADALKGTDL PSKSTHFSEI
GRAYQSIVSN GVNFQGSLQA FMDSFVLSSL KKRDMKDKAL SDPSSMKAHG AEGGEEKPSG
RSSQRKAEKS QHEPLDLSVR PDASLPGSSV TVQDSIAWHG CLFCAFTTSS MELMALHLQA
NHLGKAKRKE NAAGVAINCK EQAREVGKMA LLPTAQSNKE MGLSGMIGSL DSASEKMAQG
QAKETLGDQK SGPWPSHVDP AFCNFPSDFY KQFGVYPGVV GSGASGSCSN KDPDGKAHPE
EDAPILIPET TSKNATDDLS DIASSEDMDS FKGENNDEED IETEPEMMSK PLSALSKDSN
SDGGDSLLPT GTPQPVQGLV SPLAQASEKQ WHSPGLLPAQ DPSVGLPKPE RGPPGLEKPM
NMLSVLRAYS SDGLAAFNGL ASSTANSGCI KRPDLCGK
//
